Molecular interactions between tubulin tails and glutamylases reveal determinants of glutamylation patterns-Reference-Cited by-同舟云学术

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Molecular interactions between tubulin tails and glutamylases reveal determinants of glutamylation patterns

Published:2017-05-08 Issue:6 Volume:18 Page:1013-1026
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Natarajan Kathiresan¹²^ORCID,Gadadhar Sudarshan¹²,Souphron Judith¹²,Magiera Maria M¹²,Janke Carsten¹²^ORCID

Affiliation:

1. Institut Curie CNRS UMR 3348 PSL Research University Orsay France

2. CNRS UMR 3348 Universite Paris Sud Universite Paris‐Saclay Orsay France

Funder

Agence Nationale de la Recherche

Institut National Du Cancer

Fondation pour la Recherche Médicale

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embr.201643751

Reference55 articles.

1. The emerging role of the tubulin code: From the tubulin molecule to neuronal function and disease

2. The tubulin code: Molecular components, readout mechanisms, and functions

3. Posttranslational Glutamylation of α-tubulin

4. Polyglycylation of Tubulin: a Posttranslational Modification in Axonemal Microtubules

5. Graded Control of Microtubule Severing by Tubulin Glutamylation

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2. The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylation;2024-07-12

3. The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylation;2024-03-31

4. Towards a Long-Read Sequencing Approach for the Molecular Diagnosis of RPGRORF15 Genetic Variants;International Journal of Molecular Sciences;2023-11-28

5. Kinesin-microtubule interaction reveals the mechanism of kinesin-1 for discriminating the binding site on microtubule;Chinese Physics B;2023-10-01

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